5ju9

Structure of a beta-1,4-mannanase, SsGH134, in complex with Man3.

spinqualitylabelsall models 5ju9, resolution 1.18Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ju9 is a 1 chain structure with sequence from Streptomyces sp. NRRL B-24361. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.18Å Ligands: BMA, CL, MAN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1L1QK13_9ACTN Publication Abstract from PubMed The enzymatic cleavage of beta-1,4-mannans is achieved by endo-beta-1,4-mannanases, enzymes involved in germination of seeds and microbial hemicellulose degradation, and which have increasing industrial and consumer product applications. beta-Mannanases occur in a range of families of the CAZy sequence-based glycoside hydrolase (GH) classification scheme including families 5, 26, and 113. In this work we reveal that beta-mannanases of the newly described GH family 134 differ from other mannanase families in both their mechanism and tertiary structure. A representative GH family 134 endo-beta-1,4-mannanase from a Streptomyces sp. displays a fold closely related to that of hen egg white lysozyme but acts with inversion of stereochemistry. A Michaelis complex with mannopentaose, and a product complex with mannotriose, reveal ligands with pyranose rings distorted in an unusual inverted chair conformation. Ab initio quantum mechanics/molecular mechanics metadynamics quantified the energetically accessible ring conformations and provided evidence in support of a 1C4 --> 3H4double dagger --> 3S1 conformational itinerary along the reaction coordinate. This work, in concert with that on GH family 124 cellulases, reveals how the lysozyme fold can be co-opted to catalyze the hydrolysis of different polysaccharides in a mechanistically distinct manner. A beta-Mannanase with a Lysozyme-like Fold and a Novel Molecular Catalytic Mechanism.,Jin Y, Petricevic M, John A, Raich L, Jenkins H, Portela De Souza L, Cuskin F, Gilbert HJ, Rovira C, Goddard-Borger ED, Williams SJ, Davies GJ ACS Cent Sci. 2016 Dec 28;2(12):896-903. doi: 10.1021/acscentsci.6b00232. Epub, 2016 Nov 8. PMID:28058278 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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